KANL2_BOVIN
ID KANL2_BOVIN Reviewed; 458 AA.
AC Q2NL14; Q58D11;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=KAT8 regulatory NSL complex subunit 2;
DE AltName: Full=NSL complex protein NSL2;
DE AltName: Full=Non-specific lethal 2 homolog;
GN Name=KANSL2; Synonyms=NSL2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 9-347 (ISOFORM 2).
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
CC -!- FUNCTION: As part of the NSL complex it is involved in acetylation of
CC nucleosomal histone H4 on several lysine residues and therefore may be
CC involved in the regulation of transcription. {ECO:0000250}.
CC -!- SUBUNIT: Component of the NSL complex at least composed of MOF/KAT8,
CC KANSL1, KANSL2, KANSL3, MCRS1, PHF20, OGT1/OGT, WDR5 and HCFC1.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q2NL14-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q2NL14-2; Sequence=VSP_023264, VSP_023265;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAX46633.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BC111221; AAI11222.1; -; mRNA.
DR EMBL; BT021786; AAX46633.1; ALT_INIT; mRNA.
DR RefSeq; NP_001019742.2; NM_001024571.2. [Q2NL14-1]
DR AlphaFoldDB; Q2NL14; -.
DR STRING; 9913.ENSBTAP00000051777; -.
DR PaxDb; Q2NL14; -.
DR PRIDE; Q2NL14; -.
DR Ensembl; ENSBTAT00000053829; ENSBTAP00000051777; ENSBTAG00000002693. [Q2NL14-1]
DR Ensembl; ENSBTAT00000082063; ENSBTAP00000063451; ENSBTAG00000002693. [Q2NL14-2]
DR GeneID; 540194; -.
DR KEGG; bta:540194; -.
DR CTD; 54934; -.
DR VEuPathDB; HostDB:ENSBTAG00000002693; -.
DR eggNOG; ENOG502QTMA; Eukaryota.
DR GeneTree; ENSGT00940000155808; -.
DR HOGENOM; CLU_029808_3_0_1; -.
DR InParanoid; Q2NL14; -.
DR OMA; GYNRAET; -.
DR OrthoDB; 172254at2759; -.
DR TreeFam; TF324169; -.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000002693; Expressed in mammary gland and 105 other tissues.
DR ExpressionAtlas; Q2NL14; baseline and differential.
DR GO; GO:0015629; C:actin cytoskeleton; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0000123; C:histone acetyltransferase complex; ISS:UniProtKB.
DR GO; GO:0044545; C:NSL complex; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0043984; P:histone H4-K16 acetylation; ISS:UniProtKB.
DR GO; GO:0043981; P:histone H4-K5 acetylation; ISS:UniProtKB.
DR GO; GO:0043982; P:histone H4-K8 acetylation; ISS:UniProtKB.
DR GO; GO:0051571; P:positive regulation of histone H3-K4 methylation; IEA:Ensembl.
DR GO; GO:1900095; P:regulation of dosage compensation by inactivation of X chromosome; IEA:Ensembl.
DR InterPro; IPR026316; NSL2.
DR InterPro; IPR025927; Potential_DNA-bd.
DR PANTHER; PTHR13453; PTHR13453; 1.
DR Pfam; PF13891; zf-C3Hc3H; 2.
PE 2: Evidence at transcript level;
KW Alternative splicing; Chromatin regulator; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..458
FT /note="KAT8 regulatory NSL complex subunit 2"
FT /id="PRO_0000278290"
FT REGION 126..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 419..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..182
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 131
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H9L4"
FT MOD_RES 147
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H9L4"
FT MOD_RES 149
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H9L4"
FT MOD_RES 168
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AY70"
FT MOD_RES 172
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AY70"
FT MOD_RES 175
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AY70"
FT CROSSLNK 78
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H9L4"
FT VAR_SEQ 325..347
FT /note="HICQDTNQVLFKCCQGSEEVPCN -> QKDATAIGDLLTLYSGLMERALD
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16305752"
FT /id="VSP_023264"
FT VAR_SEQ 348..458
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16305752"
FT /id="VSP_023265"
SQ SEQUENCE 458 AA; 51208 MW; 5897007E68AE04AA CRC64;
MNRIRIHVLP TNRGRITPVP RSQEPLSCSF THRPCSQPRL EGQEFCIKHI LEDKNAPFKQ
CSYVSTKNGK RCPSAAPKPE KKDGASFCAE HARRNALALH AQMKKTSPGP VGETLLCQLS
SYAKTELGSQ TPESSRSEAS RILDEDSWSD GDQEPITVDQ TWRGDPDSEA DSIDSDQEDP
LKHAGVYTAE EVALIMREKL IRLQSLYIDQ FKRLQHLLKE KKRRYLHNRK VEHEALGSSL
LTGPEGLLAK ERENLKRLKC LRRYRQRYGV EALLHRQLKE RRMLATDGAA QQAHTTRSSQ
RCLAFVDDVR CSNQSLPMTR HCLTHICQDT NQVLFKCCQG SEEVPCNKPV PVSLSEDPCC
PLHFQLPPQM YKPEQDLDVV GDGMQCPPSP LLFDPSLTLE DHPVKEIAEG PVDILGQMQM
AGDGCRSQGP RNSEKAPAPL PQSGIATANG KPEPTSVS
